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Hang Ruan,Xuan Zhu,Zhen Zhang,Xin-fang Liang,Yan Fu,Mei-qin Su,Qi-lin Liu,Xiu-min Wang 대한약학회 2011 Archives of Pharmacal Research Vol.34 No.8
dl-Praeruptorin A (Pd-Ia) is the major active constituent of the traditional Chinese medicine Peucedanum praeruptorum Dunn. Recently it has been identified as a novel agent in the treatment and prevention of cardiovascular diseases. Accordingly, we investigated the metabolism of Pd-Ia in rat liver microsomes. The involvement of cytochrome P450 (CYP) and CYP isoforms were identified using a CYP-specific inhibitor (SKF-525A), CYP-selective inhibitors (α-naphthoflavone, metyrapone, fluvastatin, quinidine, disulfiram, ketoconazole and ticlopidine) and CYP-selective inducers (phenobarbital, dexamethasone and β-naphthoflavone). Residual concentrations of the substrate and metabolites were determined by HPLC, and further identified by their mass spectra and chromatographic behavior. These experiments showed that CYP450 is involved in Pd-Ia metabolism, and that the major CYP isoform responsible is CYP3A1/2, which acts in a concentration-dependent manner. Four Pd-Ia metabolites (M1, M2, M3, and M4) were detected after incubation with rat liver microsomes. Hydroxylation was the primary metabolic pathway of Pd-Ia, and possible chemical structures of the metabolites were identified. Further research is now needed to link the metabolism of Pd-Ia to its drug-drug interactions.
Ruan, Li-Ping,Luo, Han-Lin,Zhang, Hang-Yu,Zhao, Xiaojun The Polymer Society of Korea 2009 Macromolecular Research Vol.17 No.8
Although the existing design principle of full-sequence ionic complement is convenient for the development of peptides, it greatly constrains the exploration of peptides with other possible assembly mechanisms and different yet essential functions. Herein, a novel designed half-sequence ionic complementary peptide (referred to as P9), AC-Pro-Ser-Phe-Asn-Phe-Lys-Phe-Glu-Pro-$NH_2$, is reported. When transferred from pure water to sodium chloride solution, P9 underwent a dramatic morphological transformation from globular aggregations to nanofibers. Moreover, the rheological experiment showed that the P9 could form a hydrogel with a storage modulus of about 30 Pa even at very low peptide concentration (0.5% (wt/vol)). The P9 hydrogel formed in salt solution could recover in a period of about 1,800 sec, which is faster than that in the pure water. The data suggestcd that the half-sequence, ionic complementary peptide might be worthy of further research for its special properties.